Effect of 17O2 and 13CO on EPR espectra of nickel in hydrogenase from Chromatium vinosum

Zwaan, J.W. van der; Coremans, J. M. C. C.; Bouwens, E.C.M.; Albracht, S.P.J.

doi:10.1016/0167-4838(90)90051-g

Cited by 124 publications

(135 citation statements)

References 42 publications

Supporting

Mentioning

122

Contrasting

Unclassified

Order By: Relevance

“…Like the D. gigas enzyme (Femandez et al, 1986), the oxidized hydrogenase from C. vinosum can occur in the ready or unready state (Van der Zwaan et al, 1990). Transition of one form into the other can be obtained by complete reduction and appropriate reoxidation, as reported by Van der Zwaan et al (1990) and as further worked out by Chen (1992). An FTIR spectrum at 20 K of enzyme containing 85% Ni,(III) and 15% Ni,- Wavenumber (cm-') FIGURE 2: Absolute infrared absorbance spectrum of oxidized C.…”

Section: Resultsmentioning

confidence: 96%

“…It also shows that CO does not bind to the metals in the enzyme in this state. Oxygen, or a partly reduced oxygen species, can bind close to Ni(II1) in a very tight way (Van der Zwaan et al, 1990). It is not removed by evacuation and flushing with Ar or He, but it is fully eliminated upon reduction of the enzyme ( Van der Zwaan et al, 1990).…”

Section: Resultsmentioning

confidence: 99%

“…The enzyme was concentrated to 1.5-2.5 mM using a Centricon-30 filter. Hydrogenase was converted into a state consisting of either predominantly the Ni,(III) form or predominantly the Ni,-(111) form, as previously described (Van der Zwaan et al, 1990;Chen, 1992), and stored at or below -80 "C prior to sample manipulations.…”

Section: Methodsmentioning

confidence: 99%

“…It was first demonstrated by Van der Zwaan et al (1985) that the S = 1/2 nickel ion in this state binds hydrogen in a light-sensitive way. We will refer to nickel in this state as Ni,(I).H*, for reasons outlined by Van der Zwaan et al (1990), or as Ni-C. Upon complete reduction with €32, a state is reached where nickel is EPR-silent again.…”

mentioning

confidence: 99%

See 3 more Smart Citations

Infrared-Detectable Group Senses Changes in Charge Density on the Nickel Center in Hydrogenase from Chromatium vinosum

Bagley

Duin²,

Roseboom³

et al. 1995

Biochemistry

218

217

View full text Add to dashboard Cite

An infrared-detectable group senses changes in charge density on the nickel center in hydrogenase from Chromatium vinosum Bagley, K.A.; Duin, E.L.; Roseboom, W.; Albracht, S.P.J.; Woodruff, W.H. General rights It is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), other than for strictly personal, individual use, unless the work is under an open content license (like Creative Commons). Disclaimer/Complaints regulationsIf you believe that digital publication of certain material infringes any of your rights or (privacy) interests, please let the Library know, stating your reasons. In case of a legitimate complaint, the Library will make the material inaccessible and/or remove it from the website. Please Ask the Library: http://uba.uva.nl/en/contact, or a letter to: Library of the University of Amsterdam, Secretariat, Singel 425, 1012 WP Amsterdam, The Netherlands. You will be contacted as soon as possible. ABSTRACT: Fourier transform infrared studies of nickel hydrogenase from Chromatium vinosum reveal the presence of a set of three absorption bands in the 2100-1900 cm-1 spectral region. These bands, which do not arise from carbon monoxide, have line widths and intensities rivaling those of a band arising from the carbon monoxide stretching frequency (v(C0)) in the Ni(I1)CO species of this enzyme

show abstract

Section: Resultsmentioning

confidence: 96%

Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

Infrared-Detectable Group Senses Changes in Charge Density on the Nickel Center in Hydrogenase from Chromatium vinosum

Bagley

Duin²,

Roseboom³

et al. 1995

Biochemistry

218

217

View full text Add to dashboard Cite

show abstract

“…As in hydrogenase from Chromutium vinosum [33] the nuclear spin of ' T O introduced an isotropic hyperfine splitting [24]. Although the EPR signal of the CO-treated species shows that the unpaired electron is in an orbital with mainly dz2 character, both isotopes, ' T O and 77Se, introduced an hyperfine splitting.…”

mentioning

confidence: 99%

Changes in the Electronic Structure Around Ni in Oxidized and Reduced Selenium‐Containing Hydrogenases from Methanococcus Voltae

Sorgenfrei

Duin

Klein

et al. 1997

European Journal of Biochemistry

View full text Add to dashboard Cite

The selenium-containing F420-reducing hydrogenase from Methanococcus voltae was anaerobically purified to a specific hydrogen-uptake activity of 350 U/mg protein as determined with the natural electron acceptor. The concentrated enzyme was used for EPR-spectroscopic investigations. As isolated, the enzyme showed an EPR spectrum with gnyL values of 2.21, 2.15 and 2.01. Illumination of such samples at low temperatures led to an EPR spectrum with gxyz values of 2.05, 2.11 and 2.29. These spectra are typical for [NiFeIhydrogenases in the active state. Spectra of samples enriched in 77Se showed a hyperfine interaction between the unpaired spin of the nickel ion and the nuclear spin of one "Se atom before and after illumination. A 90" flip of the electronic z-axis is proposed to explain the hyperfine interaction in both states. This has been demonstrated previously only for the F420-non-reducing hydrogenase from M . voltue, where the selenium atom is present as a selenocysteine residue on an unusuallyThe results demonstrate that the three-dimensional structures of the active sites in the selenium-containing F420-reducing and F420-non-reducing hydrogenases from M. voltue are highly similar and hence are not influenced by the unusual subunit structure of the latter enzyme. Oxidized samples containing either natural selenium or 77Se were prepared from the F420-reducing and the selenium-containing F420-nonreducing hydrogenase. Both enzymes exhibited EPR spectra typical for [NiFeIhydrogenases in the inactive 'ready' state. In contrast to the reduced form, no splitting of the nickel-derived signal due to the nuclear spin of "Se was observed in the oxidized state, indicating that the electronic z-axis is perpendicular to the Ni-Se direction.Keywords: [NiFeIhydrogenase ; EPR ; purification ; selenium ; selenocysteine.The simplest biochemical redox reaction, namely the reversible, heterolytic cleavage of dihydrogen into two protons and two electrons is catalysed by enzymes called hydrogenases [I, 21. These are found in many organisms from all three domains, bacteria, eukarya and archaea. Different classes are defined according to the metal content of the enzymes. One class comprises hydrogenases containing no metal other than iron. These enzymes are called Fe-only hydrogenases or [Felhydrogenases [l]. The second class consists of hydrogenases that contain nickel in addition to iron. Accordingly these enzymes were named [NiFeIhydrogenases. Most of the characterized hydrogenases belong to this group. The EPR spectra of nickel respond to redox changes [4-71 and this M. voltae is an anaerobic archaeon that gains energy by oxidation of hydrogen via hydrogenases and concomitant reduction Correspondence to 0. Sorgenfrei,

show abstract

Ab initio investigation of the structural and electronic differences between active-site models of [NiFe] and [NiFeSe] hydrogenases

Gioia¹,

Fantucci²,

Guigliarelli

et al. 1999

Int. J. Quant. Chem.

View full text Add to dashboard Cite

ABSTRACT:The structural and electronic differences between coordination w x w x compounds which model NiFe and NiFeSe hydrogenase active sites were investigated using quantum chemical methods. A previous study showed that the structural and electronic properties of these model compounds are largely consistent with available w x Ž experimental data in the case of NiFe hydrogenases L. De Gioia, P. Fantucci, .

show abstract

Effect of 17O2 and 13CO on EPR espectra of nickel in hydrogenase from Chromatium vinosum

Cited by 124 publications

References 42 publications

Infrared-Detectable Group Senses Changes in Charge Density on the Nickel Center in Hydrogenase from Chromatium vinosum

Infrared-Detectable Group Senses Changes in Charge Density on the Nickel Center in Hydrogenase from Chromatium vinosum

Changes in the Electronic Structure Around Ni in Oxidized and Reduced Selenium‐Containing Hydrogenases from Methanococcus Voltae

Ab initio investigation of the structural and electronic differences between active-site models of [NiFe] and [NiFeSe] hydrogenases

Contact Info

Product

Resources

About